'Oxygen affinity' diaporamas de présentation

BIOCHEMISTRY REVIEW Session I

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Neonatal Transfusion

Neonatal Transfusion. Transfusion in the newborn requires selection of appropriate donor, measures to minimize donor exposure and prevent graft versus host disease and transmission of Cytomegalovirus. Component therapy rather than whole blood transfusion, is appropriate in most situations.

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STRUCTURE & FUNCTION OF HEMOGLOBIN

STRUCTURE & FUNCTION OF HEMOGLOBIN. DR.AMINA TARIQ BIOCHEMISTRY. GLOBULAR HEME PROTEINS. Heme proteins are a specialized group of proteins that contain heme as a Prosthetic group. Role of heme group is dictated by the environment. Examples: a. Cytochromes b. Catalase c. Hemoglobin

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Globular Proteins

Globular Proteins. UNIT I: Protein Structure and Function. Overview. This chapter examines relationship b/w structure and function for the clinically important globular hemeproteins, and mainly Hb. II. Globular hemeproteins.

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Oxygen Binding Proteins

Oxygen Binding Proteins. Objectives :. Hemoproteins carring O2 Myoglobin function and structure Hemoglobin function and structure and forms O2 binding to myoglobin and hemoglobin O2 dissociation curve Allosteric effectors. Why do we need oxygen carriers?.

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GLOBULAR HEMOPROTEINS

GLOBULAR HEMOPROTEINS. Hemeproteins are a group of specialized proteins that contain heme as a tightly bound prosthetic group. Heme is a complex of protoporphyrin IX and ferrous iron (Fe2+) .

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Oxygen Binding Proteins

Oxygen Binding Proteins. Oxygen Binding Proteins are Hemoproteins. Oxygen binding proteins ( myoglobin and hemoglobin) are hemoproteins Hemoproteins are a group of specialized proteins that contain heme as a tightly bound prosthetic group.

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BPG binds in the cavity between the ?-chains, making electrostatic interactions

BPG binds in the cavity between the ?-chains, making electrostatic interactions BPG cannot bind to the oxy form, thus functions by stabilizing the deoxy form. The decrease in oxygen affinity is explained by stabilization of deoxy-Hb.

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